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Volumn 287, Issue 27, 2012, Pages 23104-23118

Functional regulation of sugar assimilation by N-glycan-specific interaction of pancreatic α-amylase with glycoproteins of duodenal brush border membrane

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ASSAYS; BLOOD SUGARS; BRUSH BORDER MEMBRANES; CARBOHYDRATE BINDING; DOSE-DEPENDENT; ENTEROCYTES; FUNCTIONAL CHANGES; FUNCTIONAL REGULATION; GALACTANS; IMMUNOSTAINING; N-GLYCANS; SINGLE-STEP;

EID: 84863322902     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.314658     Document Type: Article
Times cited : (17)

References (54)
  • 1
    • 0027255897 scopus 로고
    • Substrate recognition at the binding site in mammalian pancreatic α- amylases
    • Ishikawa, K., Matsui, I., Kobayashi, S., Nakatani, H., and Honda, K. (1993) Substrate recognition at the binding site in mammalian pancreatic α-amylases. Biochemistry 32, 6259-6265 (Pubitemid 23196883)
    • (1993) Biochemistry , vol.32 , Issue.24 , pp. 6259-6265
    • Ishikawa, K.1    Matsui, I.2    Kobayashi, S.3    Nakatani, H.4    Honda, K.5
  • 2
    • 0027052529 scopus 로고
    • Intestinal epithelial cell surface glycosylation in mice I. Effect of high-protein diet
    • Gupta, R., Jaswal, V. M., and Meenu Mahmood, A. (1992) Intestinal epithelial cell surface glycosylation in mice. I. Effect of high protein diet. Ann. Nutr. Metab. 36, 288-295 (Pubitemid 23028442)
    • (1992) Annals of Nutrition and Metabolism , vol.36 , Issue.5-6 , pp. 288-295
    • Gupta, R.1    Jaswal, V.M.S.2    Mahmood, A.3
  • 5
    • 0021332049 scopus 로고
    • Human duodenal gland (Brunner's gland) mucus glycoprotein analysis
    • Smits, H. L., and Kramer, M. F. (1984) Human duodenal gland (Brunner's gland) mucus glycoprotein analysis. Arch. Biochem. Biophys. 228, 64-70 (Pubitemid 14175774)
    • (1984) Archives of Biochemistry and Biophysics , vol.228 , Issue.1 , pp. 64-70
    • Smits, H.L.1    Kramer, M.F.2
  • 6
    • 0027383298 scopus 로고
    • Cellular sialoglycoconjugates. A histochemical perspective
    • Roth, J. (1993) Cellular sialoglycoconjugates. A histochemical perspective. Histochem. J. 25, 687-710
    • (1993) Histochem. J. , vol.25 , pp. 687-710
    • Roth, J.1
  • 7
    • 0037085358 scopus 로고    scopus 로고
    • Porcine pancreatic α-amylase shows binding activity toward N-linked oligosaccharides of glycoproteins
    • DOI 10.1074/jbc.M105877200
    • Matsushita, H., Takenaka, M., and Ogawa, H. (2002) Porcine pancreatic α-amylase shows binding activity toward N-linked oligosaccharides of glycoproteins. J. Biol. Chem. 277, 4680-4686 (Pubitemid 34968498)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.7 , pp. 4680-4686
    • Matsushita, H.1    Takenaka, M.2    Ogawa, H.3
  • 8
    • 33646842196 scopus 로고    scopus 로고
    • Novel carbohydrate-binding activity of pancreatic trypsins to N-linked glycans of glycoproteins
    • DOI 10.1074/jbc.M513773200
    • Takekawa, H., Ina, C., Sato, R., Toma, K., and Ogawa, H. (2006) Novel carbohydrate-binding activity of pancreatic trypsins to N-linked glycans of glycoproteins. J. Biol. Chem. 281, 8528-8538 (Pubitemid 43847955)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.13 , pp. 8528-8538
    • Takekawa, H.1    Ina, C.2    Sato, R.3    Toma, K.4    Ogawa, H.5
  • 9
    • 0034712653 scopus 로고    scopus 로고
    • Subsite mapping of the human pancreatic α-amylase active site through structural, kinetic, and mutagenesis techniques
    • DOI 10.1021/bi9921182
    • Brayer, G. D., Sidhu, G., Maurus, R., Rydberg, E. H., Braun, C., Wang, Y., Nguyen, N. T., Overall, C. M., and Withers, S. G. (2000) Subsite mapping of the human pancreatic α-amylase active site through structural, kinetic, and mutagenesis techniques. Biochemistry 39, 4778-4791 (Pubitemid 30225343)
    • (2000) Biochemistry , vol.39 , Issue.16 , pp. 4778-4791
    • Brayer, G.D.1    Sidhu, G.2    Maurus, R.3    Rydberg, E.H.4    Braun, C.5    Wang, Y.6    Nguyen, N.T.7    Overall, C.M.8    Withers, S.G.9
  • 10
    • 0025855134 scopus 로고
    • A novel mannose-specific and sugar specifically aggregatable lectin from the bark of the Japanese pagoda tree (Sophora japonica)
    • Ueno, M., Ogawa, H., Matsumoto, I., and Seno, N. (1991) A novel mannose-specific and sugar specifically aggregatable lectin from the bark of the Japanese pagoda tree (Sophora japonica). J. Biol. Chem. 266, 3146-3153 (Pubitemid 21909186)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.5 , pp. 3146-3153
    • Ueno, M.1    Ogawa, H.2    Matsumoto, I.3    Seno, N.4
  • 11
    • 4744356397 scopus 로고    scopus 로고
    • Solubility-insolubility interconversion of sophoragrin, a mannose/glucose-specific lectin in Sophora japonica (Japanese pagoda tree) bark, regulated by the sugar-specific interaction
    • DOI 10.1042/BJ20040584
    • Ueda, H., Fukushima, H., Hatanaka, Y., and Ogawa, H. (2004) Solubilityinsolubility interconversion of sophoragrin, a mannose/glucose- specific lectin in Sophora japonica (Japanese pagoda tree) bark, regulated by the sugar-specific interaction. Biochem. J. 382, 821-829 (Pubitemid 39312896)
    • (2004) Biochemical Journal , vol.382 , Issue.3 , pp. 821-829
    • Ueda, H.1    Fukushima, H.2    Hatanaka, Y.3    Ogawa, H.4
  • 12
    • 0017913374 scopus 로고
    • A modified procedure for the rapid preparation of efficiently transporting vesicles from small intestinal brush border membranes. Their use in investigating some properties of D glucose and choline transport systems
    • Kessler, M., Acuto, O., Storelli, C., Murer, H.,Müller, M., and Semenza, G. (1978) A modified procedure for the rapid preparation of efficiently transporting vesicles from small intestinal brush border membranes. Their use in investigating some properties of D-glucose and choline transport systems. Biochim. Biophys. Acta 506, 136-154 (Pubitemid 8237850)
    • (1978) Biochimica et Biophysica Acta , vol.506 , Issue.1 , pp. 136-154
    • Kessler, M.1    Acuto, O.2    Storelli, C.3
  • 13
    • 0013943470 scopus 로고
    • Ultrastructural localization of alkaline phosphatase activity in the absorbing cells of the duodenum of mouse
    • Hugon, J., and Borgers, M. (1966) Ultrastructural localization of alkaline phosphatase activity in the absorbing cells of the duodenum of mouse. J. Histochem. Cytochem. 14, 629-640
    • (1966) J. Histochem. Cytochem. , vol.14 , pp. 629-640
    • Hugon, J.1    Borgers, M.2
  • 14
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Harlow, E., and Lane, D. (1988) Antibodies: A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 15
    • 72649086362 scopus 로고    scopus 로고
    • Pseudoproteoglycan (pseudoPG) probes that simulate PG macromolecular structure for screening and isolation of PG-binding proteins
    • Nakagawa, K., Nakamura, K., Haishima, Y., Yamagami, M., Saito, K., Sakagami, H., and Ogawa, H. (2009) Pseudoproteoglycan (pseudoPG) probes that simulate PG macromolecular structure for screening and isolation of PG-binding proteins. Glycoconj. J. 26, 1007-1017
    • (2009) Glycoconj. J. , vol.26 , pp. 1007-1017
    • Nakagawa, K.1    Nakamura, K.2    Haishima, Y.3    Yamagami, M.4    Saito, K.5    Sakagami, H.6    Ogawa, H.7
  • 16
    • 0014235959 scopus 로고
    • Assay of intestinal disaccharidases
    • Dahlqvist, A. (1968) Assay of intestinal disaccharidases. Anal. Biochem. 22, 99-107
    • (1968) Anal. Biochem. , vol.22 , pp. 99-107
    • Dahlqvist, A.1
  • 18
    • 0025326755 scopus 로고
    • Identification of a novel α-amylase by expression of a newly cloned human amy3 cDNA in yeast
    • DOI 10.1016/0378-1119(90)90013-H
    • Shiosaki, K., Takata, K., Omichi, K., Tomita, N., Horii, A., Ogawa, M., and Matsubara, K. (1990) Identification of a novel α-amylase by expression of a newly cloned human amy3 cDNA in yeast. Gene 89, 253-258 (Pubitemid 20206206)
    • (1990) Gene , vol.89 , Issue.2 , pp. 253-258
    • Shiosaki, K.1    Takata, K.2    Omichi, K.3    Tomita, N.4    Horii, A.5    Ogawa, M.6    Matsubara, K.7
  • 19
    • 0016754024 scopus 로고
    • Characterization studies on a new lectin found in seeds of Vicia ervilia
    • Fornstedt, N., and Porath, J. (1975) Characterization studies on a new lectin found in seeds of Vicia ervilia. FEBS Lett. 57, 187-191
    • (1975) FEBS Lett. , vol.57 , pp. 187-191
    • Fornstedt, N.1    Porath, J.2
  • 20
    • 77951849336 scopus 로고    scopus 로고
    • Loss of enteroendocrine cells in mice alters lipid absorption and glucose homeostasis and impairs postnatal survival
    • Mellitzer, G., Beucher, A., Lobstein, V., Michel, P., Robine, S., Kedinger, M., and Gradwohl, G. (2010) Loss of enteroendocrine cells in mice alters lipid absorption and glucose homeostasis and impairs postnatal survival. J. Clin. Invest. 120, 1708-1721
    • (2010) J. Clin. Invest. , vol.120 , pp. 1708-1721
    • Mellitzer, G.1    Beucher, A.2    Lobstein, V.3    Michel, P.4    Robine, S.5    Kedinger, M.6    Gradwohl, G.7
  • 23
    • 0019256425 scopus 로고
    • A fully active, two-active-site, single-chain sucrase.isomaltase from pig small intestine. Implications for the biosynthesis of a mammalian integral stalked membrane protein
    • Sjöström, H., Norén, O., Christiansen, L., Wacker, H., and Semenza, G. (1980) A fully active, two-active site, single-chain sucrase-isomaltase from pig small intestine. Implications for the biosynthesis of a mammalian integral stalked membrane protein. J. Biol. Chem. 255, 11332-11338 (Pubitemid 11134244)
    • (1980) Journal of Biological Chemistry , vol.255 , Issue.23 , pp. 11332-11338
    • Sjostrom, H.1    Noren, O.2    Christiansen, L.3
  • 24
    • 0029128989 scopus 로고
    • Localization and biosynthesis of aminopeptidase N in pig fetal small intestine
    • Danielsen, E. M., Hansen, G. H., and Niels-Christiansen, L. L. (1995) Localization and biosynthesis of aminopeptidase N in pig fetal small intestine. Gastroenterology 109, 1039-1050
    • (1995) Gastroenterology , vol.109 , pp. 1039-1050
    • Danielsen, E.M.1    Hansen, G.H.2    Niels-Christiansen, L.L.3
  • 25
    • 0030916841 scopus 로고    scopus 로고
    • Domain-specific N-glycosylation of the membrane glycoprotein dipeptidylpeptidase IV (CD26) influences its subcellular trafficking, biological stability, enzyme activity and protein folding
    • Fan, H., Meng, W., Kilian, C., Grams, S., and Reutter, W. (1997) Domainspecific N-glycosylation of the membrane glycoprotein dipeptidylpeptidase IV (CD26) influences its subcellular trafficking, biological stability, enzyme activity, and protein folding. Eur. J. Biochem. 246, 243-251 (Pubitemid 27229694)
    • (1997) European Journal of Biochemistry , vol.246 , Issue.1 , pp. 243-251
    • Fan, H.1    Meng, W.2    Kilian, C.3    Grams, S.4    Reutter, W.5
  • 26
    • 0038630508 scopus 로고    scopus 로고
    • SEA (sea-urchin sperm protein, enterokinase and agrin)-module cleavage, association of fragments and membrane targeting of rat intestinal mucin Muc3
    • DOI 10.1042/BJ20021333
    • Khatri, I. A., Wang, R., and Forstner, J. F. (2003) SEA (sea urchin sperm protein, enterokinase, and agrin)-module cleavage, association of fragments, and membrane targeting of rat intestinal mucin Muc3. Biochem. J. 372, 263-270 (Pubitemid 36609630)
    • (2003) Biochemical Journal , vol.372 , Issue.1 , pp. 263-270
    • Khatri, I.A.1    Wang, R.2    Forstner, J.F.3
  • 27
    • 78650513424 scopus 로고    scopus 로고
    • Changes in transferrin glycosylation during pregnancy may lead to false-positive carbohydrate-deficient transferrin (CDT) results in testing for riskful alcohol consumption
    • Kenan, N., Larsson, A., Axelsson, O., and Helander, A. (2011) Changes in transferrin glycosylation during pregnancy may lead to false-positive carbohydrate-deficient transferrin (CDT) results in testing for riskful alcohol consumption. Clin. Chim. Acta 412, 129-133
    • (2011) Clin. Chim. Acta , vol.412 , pp. 129-133
    • Kenan, N.1    Larsson, A.2    Axelsson, O.3    Helander, A.4
  • 28
    • 0030840995 scopus 로고    scopus 로고
    • Increased N-glycosylation and reduced transferrin-binding capacity of transferrin receptor isolated from placentae of diabetic women
    • DOI 10.1016/0143-4004(77)90011-X
    • Georgieff, M. K., Petry, C. D., Mills, M. M., McKay, H., and Wobken, J. D. (1997) Increased N-glycosylation and reduced transferrin-binding capacity of transferrin receptor isolated from placentae of diabetic women. Placenta 18, 563-568 (Pubitemid 27363979)
    • (1997) Placenta , vol.18 , Issue.7 , pp. 563-568
    • Georgieff, M.K.1    Petry, C.D.2    Mills, M.M.3    McKay, H.4    Wobken, J.D.5
  • 29
    • 0028941099 scopus 로고
    • The critical glycosylation site of human transferrin receptor contains a high mannose oligosaccharide
    • Hayes, G. R., Williams, A., Costello, C. E., Enns, C. A., and Lucas, J. J. (1995) The critical glycosylation site of human transferrin receptor contains a high mannose oligosaccharide. Glycobiology 5, 227-232
    • (1995) Glycobiology , vol.5 , pp. 227-232
    • Hayes, G.R.1    Williams, A.2    Costello, C.E.3    Enns, C.A.4    Lucas, J.J.5
  • 30
    • 0025864486 scopus 로고
    • Expression and endocytosis of integrin VLA receptors for collagen, fibronectin and laminin by normal human keratinocytes
    • Le Varlet, B., Staquet, M. J., Dezutter-Dambuyant, C., Gaucherand, M., and Schmitt, D. (1991) Expression and endocytosis of integrin VLA receptors for collagen, fibronectin and laminin by normal human keratinocytes. J. Dermatol. Sci. 2, 287-299
    • (1991) J. Dermatol. Sci. , vol.2 , pp. 287-299
    • Le Varlet, B.1    Staquet, M.J.2    Dezutter-Dambuyant, C.3    Gaucherand, M.4    Schmitt, D.5
  • 31
    • 33745902844 scopus 로고    scopus 로고
    • Molecular mechanisms of late endosome morphology, identity and sorting
    • DOI 10.1016/j.ceb.2006.06.002, PII S0955067406000780
    • Russell, M. R., Nickerson, D. P., and Odorizzi, G. (2006) Molecular mechanisms of late endosome morphology, identity and sorting. Curr. Opin. Cell Biol. 18, 422-428 (Pubitemid 44040964)
    • (2006) Current Opinion in Cell Biology , vol.18 , Issue.4 , pp. 422-428
    • Russell, M.R.G.1    Nickerson, D.P.2    Odorizzi, G.3
  • 32
    • 35348912549 scopus 로고    scopus 로고
    • Involvement of an enterocyte renin-angiotensin system in the local control of SGLT1-dependent glucose uptake across the rat small intestinal brush border membrane
    • DOI 10.1113/jphysiol.2007.138578
    • Wong, T. P., Debnam, E. S., and Leung, P. S. (2007) Involvement of an enterocyte renin-angiotensin system in the local control of SGLT1-dependent glucose uptake across the rat small intestinal brush border membrane. J. Physiol. 584, 613-623 (Pubitemid 47578343)
    • (2007) Journal of Physiology , vol.584 , Issue.2 , pp. 613-623
    • Wong, T.P.1    Debnam, E.S.2    Leung, P.S.3
  • 34
    • 33750291932 scopus 로고    scopus 로고
    • Structure of testis ACE glycosylation mutants and evidence for conserved domain movement
    • DOI 10.1021/bi061146z
    • Watermeyer, J. M., Sewell, B. T., Schwager, S. L., Natesh, R., Corradi, H. R., Acharya, K. R., and Sturrock, E. D. (2006) Structure of testis ACE glycosylation mutants and evidence for conserved domain movement. Biochemistry 45, 12654-12663 (Pubitemid 44630850)
    • (2006) Biochemistry , vol.45 , Issue.42 , pp. 12654-12663
    • Watermeyer, J.M.1    Sewell, B.T.2    Schwager, S.L.3    Natesh, R.4    Corradi, H.R.5    Acharya, K.R.6    Sturrock, E.D.7
  • 36
    • 1642534610 scopus 로고    scopus 로고
    • Crystal structure of human dipeptidyl peptidase IV in complex with a decapeptide reveals details on substrate specificity and tetrahedral intermediate formation
    • DOI 10.1110/ps.03460604
    • Aertgeerts, K., Ye, S., Tennant, M. G., Kraus, M. L., Rogers, J., Sang, B. C., Skene, R. J., Webb, D. R., and Prasad, G. S. (2004) Crystal structure of human dipeptidyl peptidase IV in complex with a decapeptide reveals details on substrate specificity and tetrahedral intermediate formation. Protein Sci. 13, 412-421 (Pubitemid 38124962)
    • (2004) Protein Science , vol.13 , Issue.2 , pp. 412-421
    • Aertgeerts, K.1    Ye, S.2    Tennant, M.G.3    Kraus, M.L.4    Rogers, J.5    Sang, B.-C.6    Skene, R.J.7    Webb, D.R.8    Prasad, G.S.9
  • 37
    • 70349304299 scopus 로고    scopus 로고
    • Basolateral internalization of GPI-anchored proteins occurs via a clathrin-independent flotillin-dependent pathway in polarized hepatic cells
    • Aït-Slimane, T., Galmes, R., Trugnan, G., and Maurice, M. (2009) Basolateral internalization of GPI-anchored proteins occurs via a clathrin-independent flotillin-dependent pathway in polarized hepatic cells. Mol. Biol. Cell 20, 3792-3800
    • (2009) Mol. Biol. Cell , vol.20 , pp. 3792-3800
    • Aït-Slimane, T.1    Galmes, R.2    Trugnan, G.3    Maurice, M.4
  • 39
    • 0022504432 scopus 로고
    • The sucrase-isomaltase complex: Primary structure, membrane-orientation, and evolution of a stalked, intrinsic brush border protein
    • Hunziker, W., Spiess, M., Semenza, G., and Lodish, H. F. (1986) The sucrase- isomaltase complex. Primary structure, membrane orientation, and evolution of a stalked, intrinsic brush border protein. Cell 46, 227-234 (Pubitemid 16031688)
    • (1986) Cell , vol.46 , Issue.2 , pp. 227-234
    • Hunziker, W.1    Spiess, M.2    Semenza, G.3    Lodish, H.F.4
  • 40
    • 77953693954 scopus 로고    scopus 로고
    • + ATPase in proximal tubule epithelial cells. Role of cytosolic phospholipase A2α and phosphatidylinositol 4-phosphate 5-kinase gamma
    • + ATPase in proximal tubule epithelial cells. Role of cytosolic phospholipase A2α and phosphatidylinositol 4-phosphate 5-kinase gamma. Biochim. Biophys. Acta 1803, 919-930
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 919-930
    • Gallicchio, M.A.1    Bach, L.A.2
  • 41
    • 78649896860 scopus 로고    scopus 로고
    • Diverse pathways for maturation of the Na,K-ATPase β1 and β2 subunits in the endoplasmic reticulum of Madin-Darby canine kidney cells
    • Tokhtaeva, E., Sachs, G., and Vagin, O. (2010) Diverse pathways for maturation of the Na,K-ATPase β1 and β2 subunits in the endoplasmic reticulum of Madin-Darby canine kidney cells. J. Biol. Chem. 285, 39289-39302
    • (2010) J. Biol. Chem. , vol.285 , pp. 39289-39302
    • Tokhtaeva, E.1    Sachs, G.2    Vagin, O.3
  • 43
    • 0033580927 scopus 로고    scopus 로고
    • Temporal association of the N- And O-linked glycosylation events and their implication in the polarized sorting of intestinal brush border sucrase-isomaltase, aminopeptidase N, and dipeptidyl peptidase IV
    • Naim, H. Y., Joberty, G., Alfalah, M., and Jacob, R. (1999) Temporal association of the N- and O-linked glycosylation events and their implication in the polarized sorting of intestinal brush border sucrase-isomaltase, aminopeptidase N, and dipeptidyl peptidase IV. J. Biol. Chem. 274, 17961-17967
    • (1999) J. Biol. Chem. , vol.274 , pp. 17961-17967
    • Naim, H.Y.1    Joberty, G.2    Alfalah, M.3    Jacob, R.4
  • 45
    • 38149128279 scopus 로고    scopus 로고
    • The influence of age on intestinal dipeptidyl peptidase IV (DPP IV/CD26), disaccharidases, and alkaline phosphatase enzyme activity in C57BL/6 mice
    • Detel, D., Baticic, L., and Varljen, J. (2008) The influence of age on intestinal dipeptidyl peptidase IV (DPP IV/CD26), disaccharidases, and alkaline phosphatase enzyme activity in C57BL/6 mice. Exp. Aging Res. 34, 49-62
    • (2008) Exp. Aging Res. , vol.34 , pp. 49-62
    • Detel, D.1    Baticic, L.2    Varljen, J.3
  • 46
    • 0019569949 scopus 로고
    • Effect dietary corn starch intake on pancreatic amylase and intestinal maltase and pH in cattle
    • Russell, J. R., Young, A. W., and Jorgensen, N. A. (1981) Effect dietary corn starch intake on pancreatic amylase and intestinal maltase and pH in cattle. J. Anim. Sci. 52, 1177-1182
    • (1981) J. Anim. Sci. , vol.52 , pp. 1177-1182
    • Russell, J.R.1    Young, A.W.2    Jorgensen, N.A.3
  • 47
    • 0014089371 scopus 로고
    • Exocrine pancreatic secretion by calves fed soybean and milk protein diets
    • Gorrill, A. D., Thomas, J. W., Stewart, W. E., and Morrill, J. L. (1967) Exocrine pancreatic secretion by calves fed soybean and milk protein diets. J. Nutr. 92, 86-92
    • (1967) J. Nutr. , vol.92 , pp. 86-92
    • Gorrill, A.D.1    Thomas, J.W.2    Stewart, W.E.3    Morrill, J.L.4
  • 49
    • 0018389608 scopus 로고
    • The mode of association of the enzyme complex sucrase isomaltase with the intestinal brush border membrane
    • Brunner, J., Hauser, H., Braun, H., Wilson, K. J., Wacker, H., O'Neill, B., and Semenza, G. (1979) The mode of association of the enzyme complex sucrase-isomaltase with the intestinal brush border membrane. J. Biol. Chem. 254, 1821-1828 (Pubitemid 9169235)
    • (1979) Journal of Biological Chemistry , vol.254 , Issue.6 , pp. 1821-1828
    • Brunner, J.1    Hauser, H.2    Braun, H.3
  • 50
    • 38449087925 scopus 로고    scopus 로고
    • Effects of Concanavalin A on intestinal brush border enzyme activity in broiler chickens
    • DOI 10.1080/00071660701713526, PII 788498979
    • Rueda, E., León, M., Castañeda, M., Mendez, A., and Michelangeli, C. (2007) Effects of concanavalin A on intestinal brush border enzyme activity in broiler chickens. Br. Poult. Sci. 48, 696-702 (Pubitemid 351437332)
    • (2007) British Poultry Science , vol.48 , Issue.6 , pp. 696-702
    • Rueda, E.1    Leon, M.2    Castaneda, M.3    Mendez, A.4    Michelangeli, C.5
  • 54
    • 33745402300 scopus 로고    scopus 로고
    • Internalization and transcytosis of pancreatic enzymes by the intestinal mucosa
    • DOI 10.1369/jhc.5A6877.2006
    • Cloutier, M., Gingras, D., and Bendayan, M. (2006) Internalization and transcytosis of pancreatic enzymes by the intestinal mucosa. J. Histochem. Cytochem. 54, 781-794 (Pubitemid 43946245)
    • (2006) Journal of Histochemistry and Cytochemistry , vol.54 , Issue.7 , pp. 781-794
    • Cloutier, M.1    Gingras, D.2    Bendayan, M.3


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